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Related Experiment Videos

C5b-9 dimer: isolation from complement lysed cells and ultrastructural identification with complement-dependent

G Biesecker, E R Podack, C A Halverson

    The Journal of Experimental Medicine
    |February 1, 1979
    PubMed
    Summary
    This summary is machine-generated.

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    The membrane attack complex (MAC) forms cell lesions, differing from fluid phase SC5b-9. This dimerized MAC structure can reinsert into membranes, mimicking complement-induced damage.

    Area of Science:

    • Immunology
    • Cell Biology
    • Biochemistry

    Background:

    • The complement system is crucial for innate immunity.
    • The terminal pathway of complement forms the membrane attack complex (MAC).
    • MAC mediates cell lysis by creating pores in target cell membranes.

    Purpose of the Study:

    • To characterize the structure and properties of the membrane attack complex (MAC) isolated from cell membranes.
    • To compare the MAC with the fluid phase terminal complement complex, SC5b-9.
    • To investigate the functional and morphological characteristics of the MAC in relation to complement-mediated cell damage.

    Main Methods:

    • Isolation of MAC from complement-lysed cells.
    • Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) for subunit analysis.

    Related Experiment Videos

  • Immunochemical analysis to confirm composition.
  • Sedimentation analysis (ultracentrifugation) to determine sedimentation coefficients.
  • Molecular weight determination.
  • Electron microscopy for ultrastructural analysis.
  • Reconstitution into phospholipid bilayers.

    • Main Results:

    • Isolated MAC and fluid phase SC5b-9 share identical subunit compositions, with MAC lacking S-protein.
    • MAC exhibits a sedimentation coefficient of 33.5 S and a molecular weight of 1.7 x 10^6 daltons, indicating it is a dimer of C5b-9 (23 S, 1.0 x 10^6 daltons).
    • The MAC dimer can convert to a monomer without subunit dissociation.
    • Electron microscopy reveals MAC possesses the characteristic morphology of complement-induced membrane lesions, unlike SC5b-9.
    • Reconstituted MAC into lipid bilayers mimics the appearance and orientation of natural complement lesions.

    Conclusions:

    • The membrane attack complex (MAC) exists as a dimer (C5b-9)2, distinct from the monomeric SC5b-9 fluid phase complex.
    • The dimeric MAC structure is responsible for the ultrastructural lesions observed in complement-mediated cell lysis.
    • The isolated MAC retains the ability to form membrane lesions upon reincorporation into lipid bilayers, validating its role in complement cytotoxicity.